FMO DATABASE

FMODB ID: Z622N

Calculation Name: 5H77-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5H77

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	84
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-517758.48088
FMO2-HF: Nuclear repulsion	484698.243183
FMO2-HF: Total energy	-33060.237696
FMO2-MP2: Total energy	-33159.433926

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)

Summations of interaction energy for fragment #1(A:4:PRO)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-0.323	2.233	1.075	-0.927	-2.704	0.001

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : -0.012

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

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X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	6	GLY	0	0.072	0.031	3.822	-0.414	0.927	-0.012	-0.485	-0.843	0.002
4	A	7	LEU	0	-0.021	-0.004	2.519	-0.461	0.587	1.088	-0.423	-1.713	-0.001
5	A	8	THR	0	0.025	0.008	4.644	0.704	0.871	-0.001	-0.019	-0.148	0.000
6	A	9	GLU	-1	-0.857	-0.941	7.320	-1.492	-1.492	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.019	0.009	7.256	0.252	0.252	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.017	-0.003	6.914	0.225	0.225	0.000	0.000	0.000	0.000
9	A	12	GLN	0	-0.007	0.008	10.055	0.247	0.247	0.000	0.000	0.000	0.000
10	A	13	GLY	0	0.013	0.012	12.563	0.117	0.117	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.016	-0.013	12.990	0.075	0.075	0.000	0.000	0.000	0.000
12	A	15	THR	0	-0.010	-0.021	13.555	0.078	0.078	0.000	0.000	0.000	0.000
13	A	16	VAL	0	-0.037	-0.017	16.075	0.060	0.060	0.000	0.000	0.000	0.000
14	A	17	GLU	-1	-0.822	-0.911	17.964	-0.256	-0.256	0.000	0.000	0.000	0.000
15	A	18	VAL	0	0.006	0.016	18.079	0.036	0.036	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.056	-0.024	20.317	0.034	0.034	0.000	0.000	0.000	0.000
17	A	20	ARG	1	0.841	0.913	21.583	0.310	0.310	0.000	0.000	0.000	0.000
18	A	21	GLN	0	-0.048	-0.045	22.326	0.027	0.027	0.000	0.000	0.000	0.000
19	A	22	GLN	0	-0.093	-0.028	24.286	0.019	0.019	0.000	0.000	0.000	0.000
20	A	23	PRO	0	-0.008	0.015	21.800	0.014	0.014	0.000	0.000	0.000	0.000
21	A	24	PRO	0	-0.003	-0.010	25.107	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.828	-0.912	22.997	-0.191	-0.191	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.033	0.004	19.108	-0.012	-0.012	0.000	0.000	0.000	0.000
24	A	27	VAL	0	0.010	0.001	18.388	-0.036	-0.036	0.000	0.000	0.000	0.000
25	A	28	GLU	-1	-0.907	-0.948	19.461	-0.194	-0.194	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.018	-0.015	19.085	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	30	ALA	0	-0.020	-0.008	15.575	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	31	VAL	0	0.007	0.003	16.542	-0.029	-0.029	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.792	-0.858	18.276	-0.217	-0.217	0.000	0.000	0.000	0.000
30	A	33	TYR	0	-0.002	-0.011	13.616	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	34	PHE	0	0.008	-0.021	11.639	-0.034	-0.034	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.030	-0.013	14.881	0.004	0.004	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.814	0.893	17.534	0.260	0.260	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.003	0.001	12.405	0.005	0.005	0.000	0.000	0.000	0.000
35	A	38	ARG	1	0.901	0.959	14.333	0.217	0.217	0.000	0.000	0.000	0.000
36	A	39	GLN	0	0.053	0.026	15.212	0.015	0.015	0.000	0.000	0.000	0.000
37	A	40	GLN	0	-0.019	-0.002	16.456	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.938	0.969	8.810	0.541	0.541	0.000	0.000	0.000	0.000
39	A	42	ALA	0	0.028	0.018	15.458	0.028	0.028	0.000	0.000	0.000	0.000
40	A	43	PHE	0	0.011	-0.006	18.156	0.022	0.022	0.000	0.000	0.000	0.000
41	A	44	TYR	0	-0.013	-0.004	16.473	0.008	0.008	0.000	0.000	0.000	0.000
42	A	45	GLU	-1	-0.923	-0.980	14.369	-0.167	-0.167	0.000	0.000	0.000	0.000
43	A	46	ILE	0	-0.007	-0.004	18.604	0.022	0.022	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.051	-0.033	21.637	0.016	0.016	0.000	0.000	0.000	0.000
45	A	48	HIS	0	-0.044	-0.003	19.598	0.020	0.020	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.008	0.005	21.715	0.014	0.014	0.000	0.000	0.000	0.000
47	A	50	PRO	0	0.000	-0.003	23.979	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	51	ASN	0	0.007	-0.008	26.875	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	52	LEU	0	0.029	0.036	26.801	0.003	0.003	0.000	0.000	0.000	0.000
50	A	53	ASN	0	0.006	0.002	29.838	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	54	GLU	-1	-0.918	-0.968	30.996	-0.060	-0.060	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.876	-0.944	31.470	-0.047	-0.047	0.000	0.000	0.000	0.000
53	A	56	GLN	0	-0.040	-0.038	31.628	0.000	0.000	0.000	0.000	0.000	0.000
54	A	57	ARG	1	0.814	0.919	25.694	0.061	0.061	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.017	-0.016	28.005	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	59	ALA	0	0.037	0.030	29.648	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	60	PHE	0	0.041	0.008	25.831	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	61	ILE	0	0.005	0.005	24.522	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	62	GLN	0	0.005	-0.001	26.443	-0.010	-0.010	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.032	-0.027	27.477	0.001	0.001	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.042	-0.012	21.393	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	65	LYS	1	0.805	0.910	24.879	0.089	0.089	0.000	0.000	0.000	0.000
63	A	66	ASP	-1	-0.908	-0.935	27.008	-0.090	-0.090	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.841	-0.928	26.258	-0.111	-0.111	0.000	0.000	0.000	0.000
65	A	68	PRO	0	-0.023	-0.011	21.186	0.001	0.001	0.000	0.000	0.000	0.000
66	A	69	SER	0	-0.082	-0.037	21.775	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	70	GLN	0	-0.001	-0.016	23.737	0.014	0.014	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.041	0.019	19.433	0.003	0.003	0.000	0.000	0.000	0.000
69	A	72	ALA	0	0.005	-0.002	19.554	0.005	0.005	0.000	0.000	0.000	0.000
70	A	73	ASN	0	0.014	0.007	20.995	0.015	0.015	0.000	0.000	0.000	0.000
71	A	74	LEU	0	0.031	0.019	23.501	0.007	0.007	0.000	0.000	0.000	0.000
72	A	75	LEU	0	0.001	0.013	17.631	0.004	0.004	0.000	0.000	0.000	0.000
73	A	76	ALA	0	-0.005	-0.005	21.959	0.011	0.011	0.000	0.000	0.000	0.000
74	A	77	GLU	-1	-0.903	-0.957	23.886	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	78	ALA	0	0.021	0.006	24.270	0.004	0.004	0.000	0.000	0.000	0.000
76	A	79	LYS	1	0.842	0.907	20.479	-0.010	-0.010	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.873	0.948	24.667	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	81	LEU	0	-0.006	-0.002	27.815	0.003	0.003	0.000	0.000	0.000	0.000
79	A	82	ASN	0	0.024	-0.016	25.467	0.001	0.001	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.889	-0.917	24.349	0.019	0.019	0.000	0.000	0.000	0.000
81	A	84	ALA	0	-0.012	-0.010	28.039	0.007	0.007	0.000	0.000	0.000	0.000
82	A	85	GLN	0	-0.043	0.019	31.284	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.000	-0.005	32.029	0.000	0.000	0.000	0.000	0.000	0.000
84	A	87	PRO	0	-0.073	-0.030	31.855	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)